Analytical Data
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Gene name
Serum Albumin/ALB
- Application
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Alternative Names
Albumin; ALB; Serum albumin; ANALBA; FDAH; PRO0883; PRO0903; PRO1341
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Species
Pig
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Source
E. coli
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Tag
N-His
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Purity
Greater than 90% as determined by SDS-PAGE.
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Uniprot
H0V003
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Expression Region
Arg19~Ala608
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Molecular Weight
70&20kDa
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Endotoxin
< 1.0 EU per μg protein as determined by the LAL method.
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Form
Freeze-dried powder
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Buffer formulation
PBS, pH7.4, containing 0.01% SKL, 1mM DTT, 5% Trehalose and Proclin300.
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Reconstitution
Reconstitute in ddH2O to a concentration of 0.1-0.5 mg/mL. Do not vortex.
- Customization
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Stability Test
The thermal stability is described by the loss rate. The loss rate was determined by accelerated thermal degradation test, that is, incubate the protein at 37℃ for 48h, and no obvious degradation and precipitation were observed. The loss rate isless than 8% within the expiration date under appropriate storage condition.
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Storage & Shelf Life
Samples are stable for up to twelve months from date of receipt at -20℃ to -80℃. Store it under sterile conditions at -20℃ to -80℃. It is recommended that the protein be aliquoted for optimal storage. Avoid repeated freeze-thaw cycles.
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Shipping
In general, recombinant proteins are supplied as lyophilized powder and shipped at ambient temperature. For bulk packages, the proteins are provided as frozen liquid and shipped with blue ice, unless otherwise requested by the customer.
Quality inspection process
Related Products
Protein Description
Serum Albumin, commonly abbreviated as ALB, is the most abundant protein in human plasma, playing a crucial role in maintaining oncotic pressure, transporting various endogenous and exogenous compounds, and modulating immune responses. Its practical applications extend into multiple fields, including clinical medicine, drug delivery systems, and biotechnology. Given its significant physiological and biochemical functions, researchers have focused on the recombinant production of ALB to overcome limitations associated with traditional extraction methods from human blood, such as variability, ethical concerns, and potential pathogen transmission. Advances in genetic engineering and protein expression technologies have enabled the development of methods to produce recombinant serum albumin in various hosts, including bacteria, yeast, and mammalian cells. This biotechnological approach not only allows for a more controlled and consistent source of albumin but also paves the way for the engineering of albumin variants with enhanced properties for therapeutic applications. Researchers are exploring modifications that can improve its stability, half-life, and binding characteristics, which could lead to more effective drug formulations. Thus, the investigation into recombinant serum albumin has garnered considerable interest, aiming to improve clinical outcomes for patients reliant on this critical protein while addressing supply shortages and enhancing therapeutic efficacy.
